ID A0A162MV67_CORDF Unreviewed; 590 AA.
AC A0A162MV67;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Isoamyl alcohol oxidase {ECO:0000313|EMBL:OAA70999.1};
GN ORFNames=LEL_09590 {ECO:0000313|EMBL:OAA70999.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA70999.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA70999.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA70999.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA70999.1}.
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DR EMBL; AZHF01000009; OAA70999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162MV67; -.
DR STRING; 1081108.A0A162MV67; -.
DR OrthoDB; 1641938at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878:SF171; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007837454"
FT DOMAIN 124..307
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 590 AA; 65023 MW; BBD7C499DA2D9C29 CRC64;
MSFLILLLLP LAFAAEAVSS NSDPGYNCRP GQGCWPSIEE WTQFNSSVGG HVYKTVPLAA
ACYKSSPYYD ENACHSIQEL YGNSTRRGEF FGQTYWLNWE TCHNTGCGLL ESDPTESLHS
SCSLGRLAAY YVDVREPSHI SAALQFAKKH NIRISIKNTG HDFYGRSSVP NTLAIWTKNL
ATMRYHANFT AHDCRAADGP NVGELGAGVI AGDAYRYFAR HGMDVTGGYE QSVGLAGGFA
QGGGVGSFTT TYGLMADNAV EFEVVTADGR LRTVNQCNDP ALFWAMRGGG GGTYAVLTKY
RVQVYPSLPI HAFEFTANFT DAGPSRDGSK NRALREILHE HARSQPAWSA QLLTGQIEYF
PERFSIKQVV PYGDDGAKLR SAMQPFYEYL NNRTDLQVIA KGYTSYANYA AYLSVTAADA
KITEPSGIFS ILASRLIPRS VFSKPETLEE LVEGVAQGIL DARKLVNRTG TQVVSETPLT
NLDVDQSTSA HPAWRDALWH VIHVGEWDAP LPERRLQDVV GPGFLKLVEP LKKLSPGGGA
YLNEANYLEP DWKQTFFGAF YDRLAAVKSK YDPTHLFDCY KCVGWRGENE
//
